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2IP1

Crystal Structure Analysis of S. cerevisiae Tryptophanyl tRNA Synthetase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004830molecular_functiontryptophan-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006436biological_processtryptophanyl-tRNA aminoacylation
A0016874molecular_functionligase activity
A1990825molecular_functionsequence-specific mRNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PG4 A 950
ChainResidue
ATYR159
AHOH792
AGLY163
ATHR196
AGLU199
AGLN312
ATYR315
AHOH515
AHOH576
AHOH721

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 A 951
ChainResidue
ATYR399
AASP409
ATYR416
AHOH738
AHOH767

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PG4 A 952
ChainResidue
AGLN240
ATYR241
AGLY243
AGLY244
AALA245
APHE246
AGLU248
APRO293
AHOH505
AHOH611

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 A 953
ChainResidue
APHE411
AGLU414
ALYS418
AGLU423
AHOH713

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues11
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Ps.SDsMHLGHM
ChainResidueDetails
APRO164-MET174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsMotif: {"description":"'HIGH' region"}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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